The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
Studies on Indole Hydroxylase
IV. Indole Hydroxylase and Aniline Hydroxylase
TORU OTANIKATSUKO AKAGIYUKIYA SAKAMOTO
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1962 Volume 52 Issue 6 Pages 428-432

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Abstract

1. Aniline hydroxylase had an optimum at pH 7.8, while that of indole hydroxylase was at pH 6.4.
2. Indole hydroxylase was less stable than aniline hydroxylase on storage.
3. In rabbit and hamster liver, indole hydroxylase was more active than aniline hydroxylase, while in guinea pig and mouse liver aniline hydroxylase was more active.
4. The degree of increase in enzyme activity after administration of methylcholanthrene differed for the two hydroxylases.
5. o-Phenanthroline strongly inhibited the hydroxylation of IBA while EDTA and KCN, which only inhibited the hydroxylation of IBA slightly, strongly inhibited that of aniline.
6. The activity of indole hydroxylase apparently decreased more than of aniline in regenerating liver.
7. It is concluded that indole hydroxylase and aniline hydroxylase are different enzymes. Indole hydroxylase is specific for indole compounds.

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© The Japanese Biochemical Society
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